Evidence map›Paper›PMID 30639111›Full record

ArticleCurrent biology : CB2019

Filopodome Mapping Identifies p130Cas as a Mechanosensitive Regulator of Filopodia Stability.

Guillaume Jacquemet, Aki Stubb, Rafael Saup, Mitro Miihkinen, Elena Kremneva, Hellyeh Hamidi, Johanna Ivaska

Open access · hybridAbstract read
In one paragraph

Article in Current biology : CB, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
9.5field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

66 citing papers in PubMed, 131 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. The role and regulation of integrins in cell migration and invasion.Nature reviews. Molecular cell biology · 2025
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review

6 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 4 institutions in 1 country.

Guillaume JacquemetTurku Centre for Biotechnology, University of Turku and Åbo Akademi University, Turku, Finland. Electronic address: guillaume.jacquemet@utu.fi.
Aki StubbTurku Centre for Biotechnology, University of Turku and Åbo Akademi University, Turku, Finland.
Rafael SaupTurku Centre for Biotechnology, University of Turku and Åbo Akademi University, Turku, Finland.
Mitro MiihkinenTurku Centre for Biotechnology, University of Turku and Åbo Akademi University, Turku, Finland.
Elena KremnevaInstitute of Biotechnology, University of Helsinki, PO Box 56, 00014 Helsinki, Finland.
Hellyeh HamidiTurku Centre for Biotechnology, University of Turku and Åbo Akademi University, Turku, Finland.
Johanna IvaskaTurku Centre for Biotechnology, University of Turku and Åbo Akademi University, Turku, Finland; Department of Biochemistry, University of Turku, Turku, Finland. Electronic address: johanna.ivaska@utu.fi.
Åbo Akademi University · FITurku Centre for Biotechnology · FIUniversity of Turku · FIUniversity of Helsinki · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Filopodia are adhesive cellular protrusions specialized in the detection of extracellular matrix (ECM)-derived cues. Although ECM engagement at focal adhesions is known to trigger the recruitment of hundreds of proteins ("adhesome") to fine-tune cellular behavior, the components of the filopodia adhesions remain undefined. Here, we performed a structured-illumination-microscopy-based screen to map the localization of 80 target proteins, linked to cell adhesion and migration, within myosin-X-induced filopodia. We demonstrate preferential enrichment of several adhesion proteins to either filopodia tips, filopodia shafts, or shaft subdomains, suggesting divergent, spatially restricted functions for these proteins. Moreover, proteins with phosphoinositide (PI) binding sites are particularly enriched in filopodia. This, together with the strong localization of PI(3,4)P

Indexed as

AnimalsCell AdhesionCell Line, TumorCrk-Associated Substrate ProteinFocal AdhesionsHumansPseudopodiaRatsBCAR1 protein, humanCrk-Associated Substrate Proteinadhesionfilopodiafilopodia tip adhesionfilopodomeintegrinmechanotransductionp130CasSIMstiffness

Identifiers

PMID30639111
PMCPMC6345628
OpenAlexW2950485114

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.